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We have previously reported that several host hnRNP proteins bind to the Sindbis virus (SINV) RNAs, and disrupting the sites of these RNA\u2013protein interactions results in decreased viral titers in tissue culture models of infection. Intriguingly, the primary molecular defect associated with the disruption of the hnRNP interactions is enhanced viral structural protein expression; however, the precise underlying mechanisms spurring the enhanced gene expression remain unknown. Moreover, our previous efforts were unable to functionally dissect whether the observed phenotypes were due to the loss of hnRNP binding or the incorporation of polymorphisms into the primary nucleotide sequence of SINV. To determine if the loss of hnRNP binding was the primary cause of attenuation or if the disruption of the RNA sequence itself was responsible for the observed phenotypes, we utilized an innovative protein tethering approach to restore the binding of the hnRNP proteins in the absence of the native interaction site. Specifically, we reconstituted the hnRNP I interaction by incorporating the 20nt bovine immunodeficiency virus transactivation RNA response (BIV-TAR) at the site of the native hnRNP I interaction sequence, which will bind with high specificity to proteins tagged with a TAT peptide. The reestablishment of the hnRNP I\u2013vRNA interaction via the BIV-TAR\/TAT tethering approach restored the phenotype back to wild-type levels. This included an apparent decrease in structural protein expression in the absence of the native primary nucleotide sequences corresponding to the hnRNP I interaction site. Collectively, the characterization of the hnRNP I interaction site elucidated the role of hnRNPs during viral infection.<\/jats:p>","DOI":"10.3390\/v14071423","type":"journal-article","created":{"date-parts":[[2022,6,29]],"date-time":"2022-06-29T03:26:37Z","timestamp":1656473197000},"page":"1423","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Binding of hnRNP I\u2013vRNA Regulates Sindbis Virus Structural Protein Expression to Promote Particle Infectivity"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8308-6916","authenticated-orcid":false,"given":"Claire E.","family":"Westcott","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, School of Medicine, University of Louisville, Louisville, KY 40202, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shefah","family":"Qazi","sequence":"additional","affiliation":[{"name":"Department of Biology, Indiana University\u2014Bloomington, Bloomington, IN 47405, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anna M.","family":"Maiocco","sequence":"additional","affiliation":[{"name":"Center for Predictive Medicine and Emerging Infectious Diseases, School of Medicine, University of Louisville, Louisville, KY 40202, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9230-4746","authenticated-orcid":false,"given":"Suchetana","family":"Mukhopadhyay","sequence":"additional","affiliation":[{"name":"Department of Biology, Indiana University\u2014Bloomington, Bloomington, IN 47405, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8728-2340","authenticated-orcid":false,"given":"Kevin J.","family":"Sokoloski","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, School of Medicine, University of Louisville, Louisville, KY 40202, USA"},{"name":"Center for Predictive Medicine and Emerging Infectious Diseases, School of Medicine, University of Louisville, Louisville, KY 40202, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2022,6,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Johansson, M.A., Powers, A.M., Pesik, N., Cohen, N.J., and Staples, J.E. 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